The DOI matches its Crossref record.
Protein Kinase C: Structure, Function, and Regulation
Open accessAbstract
The protein kinase C family of enzymes transduces the myriad of signals promoting lipid hydrolysis. The prevalence of this enzyme family in signaling is exemplified by the diverse transduction mechanisms that result in the generation of protein kinase C's activator, diacylglycerol. Signals that stimulate members of the large families of G protein-coupled receptors, tyrosine kinase receptors, or non-receptor tyrosine kinases can cause diacylglycerol production, either rapidly by activation of specific phospholipase Cs or more slowly by activation of phospholipase D to yield phosphatidic acid and then diacylglycerol(1, 2, 3).
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Cell Wall Integrity Signaling in Saccharomyces cerevisiae
Levin, D. E. (2005) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.69.2.262-291.2005 · Cited by 1,136
Molecular basis of the effects of shear stress on vascular endothelial cells
Li, Y.-S. J., Haga, J. H., & Chien, S. (2005) · Journal of Biomechanics · doi:10.1016/j.jbiomech.2004.09.030 · Cited by 904
Protein–protein interaction in insulin signaling and the molecular mechanisms of insulin resistance
Virkamäki, A., Ueki, K., & Kahn, C. R. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6609 · Cited by 854
Munc13-1 is a presynaptic phorbol ester receptor that enhances neurotransmitter release
Betz, A., Ashery, U., Rickmann, M., Augustin, I., Neher, E., Südhof, T. C., Rettig, J., & Brose, N. (1998) · Neuron · doi:10.1016/s0896-6273(00)80520-6 · Cited by 425
Mitogenic signaling via G protein-coupled receptors
van BIESEN, T., LUTTRELL, L. M., HAWES, B. E., & LEFKOWITZ, R. J. (1996) · Endocrine Reviews · doi:10.1210/edrv-17-6-698 · Cited by 361
Metadata
- Authors
- Newton, A. C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-12
- Volume
- 270
- Issue
- 48
- Pages
- 28495-28498
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2089475281
- Cited by
- 1,655
- References
- 0
- FWCI
- 32.92
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Protein Kinase C: Structure, Function, and Regulation. https://app.cochat.ai/papers/10.1074/jbc.270.48.28495
- The paper
- Newton, A. C. (1995). Protein Kinase C: Structure, Function, and Regulation. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.270.48.28495
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.